Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. VI. Amino Acids with Positively Charged Side Chains: <scp>l</scp>-Lysine and <scp>l</scp>-Arginine

“…Almost no work on Raman spectroscopy of l-lysine was published. However, Hernández et al [ 0] showed the assignment of the main modes of the Raman spectrum of l-lysine. For example, the stretching of CC is observed at 1012, 1033, 1063, and 10 6 cm l-histidine was investigated through Raman spectroscopy in a recent paper that explored the vibrational behavior of the crystal under cryogenic conditions [ 1].…”

Section: Neutral Polar Amino Acidsmentioning

confidence: 99%

Raman Spectroscopy of Amino Acid Crystals

Freire¹,

Barboza²,

Lima³

et al. 2017

Raman Spectroscopy and Applications

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In this chapter, we investigate the Raman spectra of proteinogenic amino acid crystals. Amino acids are fundamental organic molecules that compose polypeptides a linear chain of amino acids and proteins folded polypeptides with speciic functions found in all living beings. Surprisingly, the number of these basic molecules is not more than 22 20 of them commonly known as the standard amino acids, plus pyrrolysine and selenocysteine . They are deined as a molecule formed by an NH 2 group, a COOH group, a lateral chain the R group , and a hydrogen atom, all of them connected to a single carbon, the -carbon. Interestingly, -amino acids show chirality, i.e., they present diferent distributions of group of atoms around the -carbon, being deined as l-and d-form. For amino acids and proteins found in the living beings, the l-form is the dominant form, although some exceptions have been discovered in the last decades. In this chapter, we present the Raman spectra of all standard amino acids and discuss the diferent kinds of vibrations found, comparing them. As complementary part of the work, we present results on vibrational properties of some amino acids using Raman spectroscopy when subjected to speciic conditions, with variation in temperature or pressure. Finally, we present some perspectives as the investigation of purines, a group of molecules associated with the DNA molecule.

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“…30 Arginine has been shown to have two bands observed at 1586 and 1608 cm -1 due to the asymmetrical vibrations of the CN bonds of the guanidine group. Although these two overlapping bands are not always clearly observable, 3 they have been well characterized in the linear infrared spectra. 1,2,6 The interactions of these side chains with counterions and their involvement in salt bridge formation result in significant changes in the linear spectrum.…”

Section: Introductionmentioning

confidence: 99%

Identification of Arginine Residues in Peptides by 2D-IR Echo Spectroscopy

2011

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The CN stretching vibrations of the guanidyl group in the arginine dipeptide sidechain are examined by two-dimensional infrared spectroscopy. In D2O, the spectra display two distinct diagonal peaks. These nearly degenerate modes undergo ultrafast energy transfer. The energy transfer rate was determined directly from the 2D-IR spectra to be 1/2.1 ps-1. The cross peaks in 2D-IR arising from the energy transfer provide a definitive identification of arginine in larger proteins. An example of arginine in the transmembrane protein M2, found in Influenza viruses, is given.

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Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. VI. Amino Acids with Positively Charged Side Chains: l-Lysine and l-Arginine

Cited by 60 publications

References 30 publications

Raman spectra of amino acids and their aqueous solutions

Raman spectra of amino acids and their aqueous solutions

Raman Spectroscopy of Amino Acid Crystals

Identification of Arginine Residues in Peptides by 2D-IR Echo Spectroscopy

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